GenomeNet

Database: UniProt
Entry: W5TK68_9NOCA
LinkDB: W5TK68_9NOCA
Original site: W5TK68_9NOCA 
ID   W5TK68_9NOCA            Unreviewed;      1819 AA.
AC   W5TK68;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative acyl-CoA carboxylase {ECO:0000313|EMBL:AHH19559.1};
GN   ORFNames=NONO_c47750 {ECO:0000313|EMBL:AHH19559.1};
OS   Nocardia nova SH22a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH19559.1, ECO:0000313|Proteomes:UP000019150};
RN   [1] {ECO:0000313|EMBL:AHH19559.1, ECO:0000313|Proteomes:UP000019150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH22a {ECO:0000313|EMBL:AHH19559.1};
RX   PubMed=24747905;
RA   Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT   "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT   Analysis of the Complete Genome of Nocardia nova SH22a.";
RL   Appl. Environ. Microbiol. 80:3895-3907(2014).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006850; AHH19559.1; -; Genomic_DNA.
DR   RefSeq; WP_025350955.1; NZ_CP006850.1.
DR   STRING; 1415166.NONO_c47750; -.
DR   KEGG; nno:NONO_c47750; -.
DR   PATRIC; fig|1415166.3.peg.4916; -.
DR   eggNOG; COG4770; Bacteria.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_239133_0_0_11; -.
DR   OrthoDB; 4435847at2; -.
DR   Proteomes; UP000019150; Chromosome.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000019150}.
FT   DOMAIN          1..452
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          125..323
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          572..655
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1537..1819
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   1819 AA;  197631 MW;  F6868B1183DDB25D CRC64;
     MFSRIAIVNR GEAAMRLIHA VRDLAAATAR QIETVALYTD VDRNATFVRE ADIAYDLGPA
     SARPYLDLKA LEKALVTTKA DAAWVGWGFV AEDPAFAELC DHIGITFIGP SADAMRKLGD
     KIGAKLIAEE VGVPVAPWSR GAVETLDAAI AYAAEVGYPL MLKATAGGGG RGIRVITNEA
     ELVDAYERTS QEAARAFGSG VVFLERLVTG ARHVEVQVIA DGQGTAWALG VRDCSVQRRN
     QKVIEESASP VLRPEQVADL KSSAERLAVA VGYRGAATVE FLYHPGDELF AFLEVNTRLQ
     VEHPITEYTT GFDLVRAQLH VASGGRLEGE PPAERGHAIE ARLNAEDPDR DFAPAPGRIA
     LLDLPAGPGI RVDTGVSQGD TIPADFDSMI AKIIAYGSDR EQALGRLRRA VGETRVIIEG
     GATNKSFVLD LLDQPEVIDA SADTGWIDRV RGEGRLVAQR HTAVALAAAA IDAYEQEERA
     ERERLLSTAA GGRPQVQHES GRPLDLKLRG VSYRLRVARV GAHRFRIGIE AGGDIHTADV
     DLLRFDRHTG QIVVNGIRYR LVTGTHGPTI VVDVDGVTHR VSRDEGGVVR SPAPALVVAK
     PLEVGDEVEA GAPVLVLESM KMETVLRAPF KGRLKECGVS VGSQVEAGAP LLRLEPIADD
     EEDAAEAQTA DAVELDLPAA PTQVLAHDRT VRGQEDLRGL LLGFDVDPHD DRRVLADYLV
     ARKDAIADNR RPLAEELELV ELFTDLAELT HNRFRGEDAH NHVHSAREYF HTYLQSLDVE
     RAGLPEFYRA GLAKALGHYG VAELDRTPEL EAAVFRIFLA QQRPSDTVNV VTALLREWLN
     EPVPDRVLQE PVGLALERLV AATQVRFPVI ADLTRGLVYA WYGQPLLRRN RARVYSTVRK
     HLSHLDAQPD AADRSERIAE MVRSTEPLVR LLAQRLDRGI PDNTVMLEVL TRRYYGNKGL
     TGVRTEEVDG CTFVVAERRG VSLVSAAVGF DALDTVLGGL GELAGGAASI EADIYLGWEN
     QPEDFDAMAS ALQEVLGAKA LPGQVHRITA TVAGSGGAVM HHHFTFRPTS TGLVEERLIR
     GLHPYIAERM QMRRLRKFDL TRLPSSDEEV YLFQGVAKEN PADERLIAFA QVRDLTALRE
     HDGRLLSLPT AESTVATCVD SIRRAQSRRP SRKRFHTNRI VLYIWPPLDV TRAELDTIVS
     RVEPTTAGAG LEEVLLIARQ PDADTGELEK IVVRIRFDAT GGTEVTVGER TDDPVEPLDE
     YRQKVLRASS RNTVYPYELT GLLGDFAEYD LDENHALVPV DRPKGRNTAA IVAGVVSTPT
     ERHPEGVTRV VLLGDPTRSL GALSEPECRR VIAALDLAEQ MRVPLEWFSL SSGARISMKS
     GTENMDWVAA ALKRIVEFTQ DGGEINIVVS GINVGAQPYW NAEATMLMHT KGILVMTPDS
     AMVLTGKQAL DFSGGVSAED NFGIGGYDRV MGPNGQAQYW APNLAGARDV LMSHYDHTYI
     APGEATPRRA QTTDPVDRDV CAFPHIVPES DFTTVGEIFS ATANPDRKKP FDIRTVMRAL
     SDQDHPVLER WAGMADAETA VVQDAHLGGI PVCLLGIESR GVPRRGFPST DGPDTYTAGT
     LFPRSSKKAA RAINAASGNR PLVVLANLSG FDGSPESMRK LQLEYGAEIG RAIVNFRGPI
     VFCVISRYHG GAFVVFSKAL NPNMTVLALE GSFASVLGGA PAAAVVFAGE VDTRTASDPR
     VRELESRVAN ASGTERAEAS AELDELRSTV RAEKLGEVAA EFDRVHNIHR AVEVGSVDAV
     ISARELRPRI IEAIESRTA
//
DBGET integrated database retrieval system